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J. Biochem, 1988, Vol. 104, No. 5 773-776
© 1988 Japanese Biochemical Society

research-article

Purification and Characterization of Acid Phosphatase in Rat Liver Lysosomal Contents1

Masaru Himeno, Hiroshi Koutoku, Hiroshi Tsuji and Keitaro Kato2

Faculty of Pharmaceutical Sciences, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812

2 To whom correspondence should be addressed

Acid phosphatase in rat liver lysosomal contents, C-APase I, was purified about 5,700-fold over the homogenate with 8.0% recovery, to apparent homogeneity as determined from the pattern on polyacrylamide gel electrophoresis in the presence and in the absence of SDS. The purification procedures included; preparation of crude lysosomal contents, DEAE Sephacel ion exchange chromatography, hydroxylapatite chromatography, and gel filtration with Sephacryl S-300. The enzyme is composed of three identical subunits with an apparent molecular weight of 48K. The enzyme contains about 11% carbohydrate and the carbohydrate moiety was composed of mannose, fucose, N-acetylglucosamine, and N-acetylgalactosamine in a molar ratio of 20:3:11:1. Sialic acid was not detected in the enzyme. Antisera against the purified C-APase I were raised in goat and the C-APase I was rapidly purified with high yield (10%) by using the specific antibodies coupled to Sepharose 6B.

1 This study was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan.


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